Contact:
sales@biotechnologyforums.com to feature here

Thread Rating:
  • 0 Vote(s) - 0 Average
  • 1
  • 2
  • 3
  • 4
  • 5
Proteomics - New biology in the field of Science
#3
Clinical Proteomics:

The detailed information of the composition and activities of urine proteins could offer novel insights into normal renal physiology. Although proteomic studies have identified a large number of urinary proteins their practical significance remains largely unknown. Furthermore, many proteomic studies do not give explanation for post-translational modifications which may have a important impact on protein function. Many proteins are enzymes that are maintained in a latent state until their activity is compulsory. This allows for rapid host responses, without the time lag required for transcription and translation. Thus, there can be marked changes in functional states in the absence of significant alteration in concentration. These functional changes in activity are undetectable with methods that simply quantify transcript or protein levels, but are significant for characterizing the dynamic physiological standing of the host.

The activity-based protein profiling (ABPP) is a narrative move toward the assess the functional status of selected enzymes in the proteome. Activity-based protein profiling is based on the use of tagged probes that selectively respond with the active sites of a given enzyme or family of enzymes. Activity-based probes consist of a reactive group that aims the active residue of the enzyme, a short linker and reporter tag. The central premise of ABPP is that accessibility of substrate to the active site of an enzyme is an indicator of enzyme activation. Because the underlying molecular mechanisms of catalysis by members of an enzyme family are habitually identical it is possible to develop a single probe to detect the active forms of members from a given family. Members of the serine hydrolase family contribute to a serine centric charge relay system in their catalytic site and this common feature can be exploited with an activity-based probe to selectively label active serine hydrolases. Furthermore, probe-labeled enzymes can be affinity-purified through their tag and identified by mass spectrometry to determine the specific active enzymes within a biological sample.

The serine hydrolase family is one of the major enzyme classes in humans and constitutes ~1-2% of predicted protein products from the eukaryotic genome. Serine hydrolases consist of greater than 100 serine proteases and approximately 110 esterases, lipases, peptidases and amidases. While some members are well-studied (e.g. trypsin, elastase, thrombin, acetylcholinesterase), many have yet to be explained. Indeed the role for ~50% of the non-serine proteases remains undetermined, and very little is known about the occurrence and role of serine hydrolases in the urine of healthy human.
Like Post Reply
  


Messages In This Thread
RE: Proteomics - New biology in the field of Science - by brijnbhatt - 12-31-2013, 07:43 PM
Possibly Related Threads…
Thread
Author
  /  
Last Post



Users browsing this thread:
1 Guest(s)

Proteomics - New biology in the field of Science00